Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für medizinische Forschung     Collection: Jahrbuch 2012     Display Documents



ID: 638115.0, MPI für medizinische Forschung / Jahrbuch 2012
Structural Insights into the Effector − Immunity System Tse1/Tsi1 from Pseudomonas aeruginosa
Translation of Title:Structural Insights into the Effector − Immunity System Tse1/Tsi1 from Pseudomonas aeruginosa
Authors:Benz, Juliane; Sendlmeier, Christina; Barends, Thomas; Meinhart, Anton
Language:English
Date of Publication (YYYY-MM-DD):2012-07-06
Title of Journal:PLoS ONE
Journal Abbrev.:PLoS ONE
Volume:7
Issue / Number:7
Start Page:1
End Page:10
Sequence Number of Article:e40453
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:During an interbacterial battle, the type−6−secretion−system (T6SS) of the human pathogen Pseudomonas aeruginosa injects the peptidoglycan(PG)−hydrolase Tse1 into the periplasm of Gram−negative enemy cells and induces their lysis. However, for its own benefit, P. aeruginosa produces and transports the immunity−protein Tsi1 into its own periplasm where in prevents accidental exo− and endogenous intoxication. Here we present the high−resolution X−ray crystal structure of the lytic enzyme Tse1 and describe the mechanism by which Tse1 cleaves the γ−D−glutamyl−L−meso−diaminopimelic acid amide bond of crosslinked PG. Tse1 belongs to the superfamily of N1pC/P60 peptidases but is unique among described members of this family of which the structure was described, since it is a single domain protein without any putative localization domain. Most importantly, we present the crystal structure of Tse1 bound to its immunity−protein Tsi1 as well and describe the mechanism of enzyme inhibition. Tsi1 occludes the active site of Tse1 and abolishes its enzyme activity by forming a hydrogen bond to a catalytically important histidine residue in Tse1. Based on our structural findings in combination with a bioinfomatic approach we also identified a related system in Burkholderia phytofirmans. Not only do our findings point to a common catalytic mechanism of the Tse1 PG−hydrolases, but we can also show that it is distinct from other members of this superfamily. Furthermore, we provide strong evidence that the mechanism of enzyme inhibition between Tsi1 orthologues is conserved. This work is the first structural description of an entire effector/immunity pair injected by the T6SS system. Moreover, it is also the first example of a member of the N1pC/P60 superfamily which becomes inhibited upon binding to its cognate immunity protein
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Heme and Flavin Enzymes
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/mRNA Processing
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Coherent diffractive imaging
Identifiers:LOCALID:7814
URI:http%3A%2F%2Fwww.plosone.org%2Farticle%2FfetchObje...
URI:http%3A%2F%2Fwww.plosone.org%2Farticle%2Finfo%253A...
DOI:10.1371%2Fjournal.pone.0040453
Full Text:
Sorry, no privileges
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.